Structure of PDB 2cev Chain D

Receptor sequence

>2cevD (length=298) Species: 33931 ([Bacillus] caldovelox)

KPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIPI
GKAERLHEQGDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHSI
AIGTLAGVAKHYERLGVIWYDAHGDVNTAETSPSGNIHGMPLAASLGFGH
PALTQIGGYSPKIKPEHVVLIGVRSLDEGEKKFIREKGIKIYTMHEVDRL
GMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGTPVIGGLTYRES
HLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM

3D structure

• PDB: 2cev Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily.
• Chain: D
• Resolution: 2.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H99 D122 H124 D126 H139 D226 D228 E271
• Catalytic site (residue number reindexed from 1): H98 D121 H123 D125 H138 D225 D227 E270
• Enzyme Commision number: 3.5.3.1: arginase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MN	D	H99 D122 D126 D226	H98 D121 D125 D225
BS02	MN	D	D122 H124 D226 D228	D121 H123 D225 D227
BS03	GAI	D	H252 E256	H251 E255

Gene Ontology

Molecular Function

• GO:0004053 arginase activity
• GO:0016787 hydrolase activity
• GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
• GO:0030145 manganese ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0000050 urea cycle
• GO:0006525 arginine metabolic process
• GO:0019547 arginine catabolic process to ornithine

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2cev, PDBe:2cev, PDBj:2cev
• PDBsum: 2cev
• PubMed: 10196128
• UniProt: P53608|ARGI_BACCD Arginase (Gene Name=rocF)